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Mauricio J. Reginato

Researcher at Drexel University

Publications -  65
Citations -  6555

Mauricio J. Reginato is an academic researcher from Drexel University. The author has contributed to research in topics: Cancer & Signal transduction. The author has an hindex of 34, co-authored 60 publications receiving 5880 citations. Previous affiliations of Mauricio J. Reginato include Thomas Jefferson University & Harvard University.

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The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini.

TL;DR: In vitro three-dimensional epithelial cell cultures are utilized to analyze the role of apoptosis in the formation and maintenance of a hollow glandular architecture and show that apoptosis can counteract increased proliferation to maintain luminal space.
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Transcriptional Activation by Peroxisome Proliferator-activated Receptor γ Is Inhibited by Phosphorylation at a Consensus Mitogen-activated Protein Kinase Site

TL;DR: Investigating a potential mechanism whereby transcriptional activation by PPARγ may be modulated by growth factor or cytokine-stimulated signal transduction pathways involved in adipogenesis finds phosphorylation of a mitogen-activated protein kinase site in the A/B region ofPPARγ inhibits both ligand-independent and lig and-dependent transactivation functions.
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Integrins and EGFR coordinately regulate the pro-apoptotic protein Bim to prevent anoikis.

TL;DR: Bim functions as a key sensor of integrin and growth factor signals to the Erk pathway, and loss of such coordinate regulation may contribute to tumour progression.
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Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1.

TL;DR: Findings identify O-GlcNAc as a novel mechanism through which alterations in glucose metabolism regulate cancer growth and invasion and suggest that OGT may represent novel therapeutic targets for breast cancer.
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Interdomain communication regulating ligand binding by PPAR-γ

TL;DR: The ability of the A/B domain to regulate ligand binding has important implications for the evaluation and mechanism of action of potentially therapeutic ligands that bind PPAR-γ and that are likely to extend to other members of the nuclear-receptor superfamily.